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PLANT PROTEIN SERINE/THREONINE KINASES: Classification and Functions.

Annual review of plant physiology and plant molecular biology

Hardie DG.
PMID: 15012205
Annu Rev Plant Physiol Plant Mol Biol. 1999 Jun;50:97-131. doi: 10.1146/annurev.arplant.50.1.97.

The first plant protein kinase sequences were reported as recently as 1989, but by mid-1998 there were more than 500, including 175 in Arabidopsis thaliana alone. Despite this impressive pace of discovery, progress in understanding the detailed functions of...

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Hardie DG. PLANT PROTEIN SERINE/THREONINE KINASES: Classification and Functions. Annu Rev Plant Physiol Plant Mol Biol. 1999;50:97-131doi: 10.1146/annurev.arplant.50.1.97.
Hardie, D. G. (1999). PLANT PROTEIN SERINE/THREONINE KINASES: Classification and Functions. Annual review of plant physiology and plant molecular biology, 5097-131. https://doi.org/10.1146/annurev.arplant.50.1.97
Hardie, D. G.. "PLANT PROTEIN SERINE/THREONINE KINASES: Classification and Functions." Annual review of plant physiology and plant molecular biology vol. 50 (1999): 97-131. doi: https://doi.org/10.1146/annurev.arplant.50.1.97
Hardie DG. PLANT PROTEIN SERINE/THREONINE KINASES: Classification and Functions. Annu Rev Plant Physiol Plant Mol Biol. 1999 Jun;50:97-131. doi: 10.1146/annurev.arplant.50.1.97. PMID: 15012205.
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Properties of FDA-approved small molecule phosphatidylinositol 3-kinase inhibitors prescribed for the treatment of malignancies.

Pharmacological research

Roskoski R.
PMID: 33774181
Pharmacol Res. 2021 Jun;168:105579. doi: 10.1016/j.phrs.2021.105579. Epub 2021 Mar 26.

The discovery of the phosphatidylinositol 3-kinase (PI 3-kinase) pathway was a major advance in understanding eukaryotic signal transduction. The high frequency of PI 3-kinase pathway mutations in many cancers stimulated the development of drugs targeting these oncogenic mutants. The...

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Roskoski R. Properties of FDA-approved small molecule phosphatidylinositol 3-kinase inhibitors prescribed for the treatment of malignancies. Pharmacol Res. 2021;168:105579doi: 10.1016/j.phrs.2021.105579.
Roskoski, R. (2021). Properties of FDA-approved small molecule phosphatidylinositol 3-kinase inhibitors prescribed for the treatment of malignancies. Pharmacological research, 168105579. https://doi.org/10.1016/j.phrs.2021.105579
Roskoski, Robert. "Properties of FDA-approved small molecule phosphatidylinositol 3-kinase inhibitors prescribed for the treatment of malignancies." Pharmacological research vol. 168 (2021): 105579. doi: https://doi.org/10.1016/j.phrs.2021.105579
Roskoski R. Properties of FDA-approved small molecule phosphatidylinositol 3-kinase inhibitors prescribed for the treatment of malignancies. Pharmacol Res. 2021 Jun;168:105579. doi: 10.1016/j.phrs.2021.105579. Epub 2021 Mar 26. PMID: 33774181.
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Mouse models of PAK function.

Cellular logistics

Kelly ML, Chernoff J.
PMID: 23162740
Cell Logist. 2012 Apr 01;2(2):84-88. doi: 10.4161/cl.21381.

p21-activated kinases are a family of highly conserved protein serine/threonine kinases that are increasingly recognized as playing essential roles in a variety of key signaling processes. Genetic analyses in mice, using constitutive or regulated gene disruption, have provided important...

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Kelly ML, Chernoff J. Mouse models of PAK function. Cell Logist. 2012;2(2):84-88doi: 10.4161/cl.21381.
Kelly, M. L., & Chernoff, J. (2012). Mouse models of PAK function. Cellular logistics, 2(2), 84-88. https://doi.org/10.4161/cl.21381
Kelly, Mollie L, and Chernoff, Jonathan. "Mouse models of PAK function." Cellular logistics vol. 2,2 (2012): 84-88. doi: https://doi.org/10.4161/cl.21381
Kelly ML, Chernoff J. Mouse models of PAK function. Cell Logist. 2012 Apr 01;2(2):84-88. doi: 10.4161/cl.21381. PMID: 23162740; PMCID: PMC3490966.
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Recent progress towards the identification of selective inhibitors of serine/threonine protein kinases.

Current opinion in drug discovery & development

Adams JL, Lee D.
PMID: 19649935
Curr Opin Drug Discov Devel. 1999 Mar;2(2):96-109.

Protein serine/threonine kinases figure prominently among the molecular targets currently being pursued by the pharmaceutical industry. Given the conserved tertiary structure and catalytic mechanism of the mammalian kinase superfamily, it is not surprising that the discovery of selective inhibitors...

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Adams JL, Lee D. Recent progress towards the identification of selective inhibitors of serine/threonine protein kinases. Curr Opin Drug Discov Devel. 1999;2(2):96-109
Adams, J. L., & Lee, D. (1999). Recent progress towards the identification of selective inhibitors of serine/threonine protein kinases. Current opinion in drug discovery & development, 2(2), 96-109.
Adams, J L, and Lee, D. "Recent progress towards the identification of selective inhibitors of serine/threonine protein kinases." Current opinion in drug discovery & development vol. 2,2 (1999): 96-109.
Adams JL, Lee D. Recent progress towards the identification of selective inhibitors of serine/threonine protein kinases. Curr Opin Drug Discov Devel. 1999 Mar;2(2):96-109. PMID: 19649935.
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Effect of lectins on protein kinase activity.

Methods in molecular medicine

Sada K, Yamamura H.
PMID: 21374480
Methods Mol Med. 1998;9:423-32. doi: 10.1385/0-89603-396-1:423.

Protein kinases have critical roles for the amplification and distribution of the signals that are sent from the cell surface to the cytoplasm after ligand binding. They are generally classified into two groups: protein-serine/threonine kinases, such as cAMP-dependent protein...

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Sada K, Yamamura H. Effect of lectins on protein kinase activity. Methods Mol Med. 1998;9:423-32doi: 10.1385/0-89603-396-1:423.
Sada, K., & Yamamura, H. (1998). Effect of lectins on protein kinase activity. Methods in molecular medicine, 9423-32. https://doi.org/10.1385/0-89603-396-1:423
Sada, K, and Yamamura, H. "Effect of lectins on protein kinase activity." Methods in molecular medicine vol. 9 (1998): 423-32. doi: https://doi.org/10.1385/0-89603-396-1:423
Sada K, Yamamura H. Effect of lectins on protein kinase activity. Methods Mol Med. 1998;9:423-32. doi: 10.1385/0-89603-396-1:423. PMID: 21374480.
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ROCK activity regulates functional tight junction assembly during blastocyst formation in porcine parthenogenetic embryos.

PeerJ

Kwon J, Kim NH, Choi I.
PMID: 27077008
PeerJ. 2016 Apr 11;4:e1914. doi: 10.7717/peerj.1914. eCollection 2016.

The Rho-associated coiled-coil-containing protein serine/threonine kinases 1 and 2 (ROCK1 and ROCK2) are Rho subfamily GTPase downstream effectors that regulate cell migration, intercellular adhesion, cell polarity, and cell proliferation by stimulating actin cytoskeleton reorganization. Inhibition of ROCK proteins affects...

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Kwon J, Kim NH, Choi I. ROCK activity regulates functional tight junction assembly during blastocyst formation in porcine parthenogenetic embryos. PeerJ. 2016;4:e1914doi: 10.7717/peerj.1914.
Kwon, J., Kim, N. H., & Choi, I. (2016). ROCK activity regulates functional tight junction assembly during blastocyst formation in porcine parthenogenetic embryos. PeerJ, 4e1914. https://doi.org/10.7717/peerj.1914
Kwon, Jeongwoo, et al. "ROCK activity regulates functional tight junction assembly during blastocyst formation in porcine parthenogenetic embryos." PeerJ vol. 4 (2016): e1914. doi: https://doi.org/10.7717/peerj.1914
Kwon J, Kim NH, Choi I. ROCK activity regulates functional tight junction assembly during blastocyst formation in porcine parthenogenetic embryos. PeerJ. 2016 Apr 11;4:e1914. doi: 10.7717/peerj.1914. eCollection 2016. PMID: 27077008; PMCID: PMC4830244.
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Protein phosphatases in TLR signaling.

Cell communication and signaling : CCS

Seumen CHT, Grimm TM, Hauck CR.
PMID: 33882943
Cell Commun Signal. 2021 Apr 21;19(1):45. doi: 10.1186/s12964-021-00722-1.

Toll-like receptors (TLRs) are critical sensors for the detection of potentially harmful microbes. They are instrumental in initiating innate and adaptive immune responses against pathogenic organisms. However, exaggerated activation of TLR receptor signaling can also be responsible for the...

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Seumen CHT, Grimm TM, Hauck CR. Protein phosphatases in TLR signaling. Cell Commun Signal. 2021;19(1):45doi: 10.1186/s12964-021-00722-1.
Seumen, C. H. T., Grimm, T. M., & Hauck, C. R. (2021). Protein phosphatases in TLR signaling. Cell communication and signaling : CCS, 19(1), 45. https://doi.org/10.1186/s12964-021-00722-1
Seumen, Clovis H T, et al. "Protein phosphatases in TLR signaling." Cell communication and signaling : CCS vol. 19,1 (2021): 45. doi: https://doi.org/10.1186/s12964-021-00722-1
Seumen CHT, Grimm TM, Hauck CR. Protein phosphatases in TLR signaling. Cell Commun Signal. 2021 Apr 21;19(1):45. doi: 10.1186/s12964-021-00722-1. PMID: 33882943; PMCID: PMC8058998.
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Corrigendum to "Targeting ERK1/2 protein-serine/threonine kinases in human cancers" [Pharmcol. Res. 142 (2019) 151-168].

Pharmacological research

Roskoski R.
PMID: 30952557
Pharmacol Res. 2019 May;143:206. doi: 10.1016/j.phrs.2019.03.019. Epub 2019 Apr 03.

No abstract available.

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Roskoski R. Corrigendum to "Targeting ERK1/2 protein-serine/threonine kinases in human cancers" [Pharmcol. Res. 142 (2019) 151-168]. Pharmacol Res. 2019;143:206doi: 10.1016/j.phrs.2019.03.019.
Roskoski, R. (2019). Corrigendum to "Targeting ERK1/2 protein-serine/threonine kinases in human cancers" [Pharmcol. Res. 142 (2019) 151-168]. Pharmacological research, 143206. https://doi.org/10.1016/j.phrs.2019.03.019
Roskoski, Robert. "Corrigendum to "Targeting ERK1/2 protein-serine/threonine kinases in human cancers" [Pharmcol. Res. 142 (2019) 151-168]." Pharmacological research vol. 143 (2019): 206. doi: https://doi.org/10.1016/j.phrs.2019.03.019
Roskoski R. Corrigendum to "Targeting ERK1/2 protein-serine/threonine kinases in human cancers" [Pharmcol. Res. 142 (2019) 151-168]. Pharmacol Res. 2019 May;143:206. doi: 10.1016/j.phrs.2019.03.019. Epub 2019 Apr 03. PMID: 30952557.
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Cloning and partial sequencing of a novel human activin receptor-like kinase.

Oncology reports

Ohno T, Imai A, Takagi A, Horibe S, Takagi H, Tamaya T.
PMID: 21590252
Oncol Rep. 1997 Nov-Dec;4(6):1349-51. doi: 10.3892/or.4.6.1349.

Receptors for the transforming growth factor (TGF)-beta receptor superfamily are transmembrane protein serine/threonine kinases. By using a polymerase chain reaction (PCR)-based strategy to screen for the protein kinase sequences, we isolated a novel complementary DNA (cDNA) clone from a...

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Ohno T, Imai A, Takagi A, et al. Cloning and partial sequencing of a novel human activin receptor-like kinase. Oncol Rep. 1997;4(6):1349-51doi: 10.3892/or.4.6.1349.
Ohno, T., Imai, A., Takagi, A., Horibe, S., Takagi, H., & Tamaya, T. (1997). Cloning and partial sequencing of a novel human activin receptor-like kinase. Oncology reports, 4(6), 1349-51. https://doi.org/10.3892/or.4.6.1349
Ohno, T, et al. "Cloning and partial sequencing of a novel human activin receptor-like kinase." Oncology reports vol. 4,6 (1997): 1349-51. doi: https://doi.org/10.3892/or.4.6.1349
Ohno T, Imai A, Takagi A, Horibe S, Takagi H, Tamaya T. Cloning and partial sequencing of a novel human activin receptor-like kinase. Oncol Rep. 1997 Nov-Dec;4(6):1349-51. doi: 10.3892/or.4.6.1349. PMID: 21590252.
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Showing 1 to 9 of 9 entries